2myp: Difference between revisions

Latest revision as of 10:03, 1 May 2024

An arsenate reductase in the phosphate binding stateAn arsenate reductase in the phosphate binding state

Structural highlights

2myp is a 1 chain structure with sequence from Synechocystis sp. PCC 6803 substr. Kazusa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARSC_SYNY3 Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.^[1] ^[2] ^[3]

References

↑ Li R, Haile JD, Kennelly PJ. An arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a novel combination of catalytic characteristics. J Bacteriol. 2003 Dec;185(23):6780-9. PMID:14617642
↑ Lopez-Maury L, Sanchez-Riego AM, Reyes JC, Florencio FJ. The glutathione/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. strain PCC 6803. J Bacteriol. 2009 Jun;191(11):3534-43. doi: 10.1128/JB.01798-08. Epub 2009 Mar, 20. PMID:19304854 doi:http://dx.doi.org/10.1128/JB.01798-08
↑ Kim SG, Chung JS, Sutton RB, Lee JS, Lopez-Maury L, Lee SY, Florencio FJ, Lin T, Zabet-Moghaddam M, Wood MJ, Nayak K, Madem V, Tripathy JN, Kim SK, Knaff DB. Redox, mutagenic and structural studies of the glutaredoxin/arsenate reductase couple from the cyanobacterium Synechocystis sp. PCC 6803. Biochim Biophys Acta. 2012 Feb;1824(2):392-403. Epub 2011 Oct 29. PMID:22155275 doi:10.1016/j.bbapap.2011.10.012

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OCA

[1] Li R, Haile JD, Kennelly PJ. An arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a novel combination of catalytic characteristics. J Bacteriol. 2003 Dec;185(23):6780-9. PMID:14617642

[2] Lopez-Maury L, Sanchez-Riego AM, Reyes JC, Florencio FJ. The glutathione/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. strain PCC 6803. J Bacteriol. 2009 Jun;191(11):3534-43. doi: 10.1128/JB.01798-08. Epub 2009 Mar, 20. PMID:19304854 doi:http://dx.doi.org/10.1128/JB.01798-08

[3] Kim SG, Chung JS, Sutton RB, Lee JS, Lopez-Maury L, Lee SY, Florencio FJ, Lin T, Zabet-Moghaddam M, Wood MJ, Nayak K, Madem V, Tripathy JN, Kim SK, Knaff DB. Redox, mutagenic and structural studies of the glutaredoxin/arsenate reductase couple from the cyanobacterium Synechocystis sp. PCC 6803. Biochim Biophys Acta. 2012 Feb;1824(2):392-403. Epub 2011 Oct 29. PMID:22155275 doi:10.1016/j.bbapap.2011.10.012

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2myp is ON HOLD  until Paper Publication
+==An arsenate reductase in the phosphate binding state==
+<StructureSection load='2myp' size='340' side='right'caption='[[2myp]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2myp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYP FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myp OCA], [https://pdbe.org/2myp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myp RCSB], [https://www.ebi.ac.uk/pdbsum/2myp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myp ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ARSC_SYNY3 ARSC_SYNY3] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref>
-Authors: Jin, C., Yu, C., Hu, C., Hu, Y.
+==See Also==
+*[[Arsenate reductase 3D structures|Arsenate reductase 3D structures]]
-Description: An arsenate reductase in the phosphate binding state
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Hu, Y]]
+__TOC__
-[[Category: Yu, C]]
+</StructureSection>
-[[Category: Jin, C]]
+[[Category: Large Structures]]
-[[Category: Hu, C]]
+[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]]
+[[Category: Hu C]]
+[[Category: Hu Y]]
+[[Category: Jin C]]
+[[Category: Yu C]]

2myp: Difference between revisions

Latest revision as of 10:03, 1 May 2024

An arsenate reductase in the phosphate binding stateAn arsenate reductase in the phosphate binding state

Structural highlights

Function

See Also

References

Contents

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2myp: Difference between revisions

Latest revision as of 10:03, 1 May 2024

An arsenate reductase in the phosphate binding stateAn arsenate reductase in the phosphate binding state

Structural highlights

Function

See Also

References

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